The proposed research is an investigation of polyfunctional catalysis as a basis for the remarkable activity and specificity of enzymes. The proposed polyfunctional catalysts (enzyme models) are compounds that can form a covalent bond to a carbonyl group in a substrate. In so doing the catalyst not only binds the substrate but also changes the chemical nature of one of its functional groups in such a way as to increase its reactivity in the desired reaction. A second, basic functional group in the catalyst then brings about reaction by abstracting a proton from the activated bound substrate. A major point of the research is obtaining catalysts whose functional groups have the proper relative geometric orientation. Some of the proposed catalysts are of the type B-R-NH2, where B is the basic group and R is the molecular framework joining B to the amino group. These catalysts react with carbonyl substrates to give imines, which are in equilibrium with the corresponding iminium ions, and may act as epimerases, aldolases, carboxylases, etc. Other catalysts are of the type B-R0Y-H, where Y is NH, S, or O. These add -Y-H to the carbonyl group of a substrate and cleave the group X with its bonding electron pair from a compound of the type RCOX. They may act as Beta-ketothiolases, glyoxalases, amidases, esterases, etc.